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Selection of phages and conditions for the safe phage therapy against Pseudomonas aeruginosa infections

Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity

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Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity

Content Provider	Springer Nature Link
Author	Huang, Yanling Yang, Hang Yu, Junping Wei, Hongping
Copyright Year	2015
Abstract	The novel phage lysin PlySs2, is reported to be highly active against various bacteria, including staphylococci, streptococci and Listeria. However, the molecular mechanisms underlying its broad lytic spectrum remain to be established. In the present study, the lytic activity of the catalytic domain (CD, PlySc) and binding specificity of the cell wall binding domain (CBD, PlySb) of PlySs2 were examined. Our results showed that PlySc alone maintains very limited lytic activity. Enhanced green fluorescent protein (EGFP)-fused PlySb displayed high binding affinity to the streptococcal strains tested, including S. suis, S. dysgalactiae, and S. agalactiae, but not staphylococci, supporting its utility as a good CBD donor for streptococcal-targeted lysin engineering. EGFP-fused intact PlySs2 similarly displayed high affinity for streptococci, but not staphylococci. Notably, four truncated PlySb fragments showed no binding capacity. These findings collectively indicate that integrity of the PlySc and PlySb domains is an essential determinant of the broad lytic activity of PlySs2.
Starting Page	45
Ending Page	51
Page Count	7
File Format	PDF
ISSN	16740769
Journal	Virologica Sinica
Volume Number	30
Issue Number	1
e-ISSN	1995820X
Language	English
Publisher	Wuhan Institute of Virology, CAS
Publisher Date	2015-02-04
Publisher Place	Heidelberg
Access Restriction	Subscribed
Subject Keyword	streptococci lysin cell wall binding domain catalytic domain bacterial resistance Virology Medical Microbiology Oncology Biochemistry Microbiology Microbial Genetics and Genomics
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Virology Immunology Molecular Medicine

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Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity

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Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity

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Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity

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Molecular dissection of phage lysin PlySs2: integrity of the catalytic and cell wall binding domains is essential for its broad lytic activity